|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
5-512 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 897.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 5 TFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWA 84
Cdd:PRK11893 2 KFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 85 TLNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFDEKEttLGEDGIRREPLGSPVEWVEEESY 164
Cdd:PRK11893 82 ALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESE--LIEDGYRCPPTGAPVEWVEEESY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 165 FFRLSAYGDRLLAHYEANPGFILPAERRNEVASFVKSGLRDLSISRTTFDWGVPVPNDPKHIMYVWVDALTNYLTAAGYP 244
Cdd:PRK11893 160 FFRLSKYQDKLLELYEANPDFIQPASRRNEVISFVKSGLKDLSISRTNFDWGIPVPGDPKHVIYVWFDALTNYLTALGYP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 245 DESAE----RWKYWPADIHMIGKDIVRFHAVYWPAFLMSADIELPKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAKYGL 320
Cdd:PRK11893 240 DDEELlaelFNKYWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 321 DAMRYYFLREVSFGSDGSYNHEAIVNRINADLANDLGNLAQRSLSMVAKNCDGQVPAPGELTDEDNAILGAADALLDTSR 400
Cdd:PRK11893 320 DAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVPEPGALTEADEALLEAAAALLERVR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 401 AAMDDQAIHQMLNAVWQVVADANRYFAGQEPWALRKTDPARMATVLYVTIEVVRQVAILAQPVMPASSEKLLDLLGLHAE 480
Cdd:PRK11893 400 AAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEED 479
|
490 500 510
....*....|....*....|....*....|...
gi 1839969221 481 -GRSFEQLgAYGRLAAGTALPAPEGVFPRYVEK 512
Cdd:PRK11893 480 eNRDFAAL-SWGRLAPGTTLPKPEPIFPRLEEE 511
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
1-514 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 817.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 1 MSRPTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFK 80
Cdd:PRK12267 1 MMKKTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 81 DLWATLNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFDEKEttLGEDGIrrEPL-GSPVEWV 159
Cdd:PRK12267 81 ELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQ--LVDGGK--CPDcGREVELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 160 EEESYFFRLSAYGDRLLAHYEANPGFILPAERRNEV-ASFVKSGLRDLSISRTTFDWGVPVPNDPKHIMYVWVDALTNYL 238
Cdd:PRK12267 157 KEESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMiNNFIKPGLEDLSISRTSFDWGIPVPFDPKHVVYVWIDALLNYI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 239 TAAGYPDESAERW-KYWPADIHMIGKDIVRFHAVYWPAFLMSADIELPKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAK 317
Cdd:PRK12267 237 TALGYGSDDDELFkKFWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 318 YGLDAMRYYFLREVSFGSDGSYNHEAIVNRINADLANDLGNLAQRSLSMVAKNCDGQVPAPGELTDEDNAILGAADALLD 397
Cdd:PRK12267 317 YGLDALRYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNRTVAMINKYFDGEIPAPGNVTEFDEELIALAEETLK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 398 TSRAAMDDQAIHQMLNAVWQVVADANRYFAGQEPWALRK--TDPARMATVLYVTIEVVRQVAILAQPVMPASSEKLLDLL 475
Cdd:PRK12267 397 NYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKdeGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQL 476
|
490 500 510
....*....|....*....|....*....|....*....
gi 1839969221 476 GLHAEGRSFEQLGAYGRLAAGTALPAPEGVFPRYVEKDE 514
Cdd:PRK12267 477 GLEEELTSWESLLEWGGLPAGTKVAKGEPLFPRIDVEEE 515
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
4-516 |
0e+00 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 784.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 4 PTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLW 83
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 84 ATLNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFD---------------------EKETTL 142
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPdryvegtcpkcgaedaygdqcENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 143 GEDGIRREPL----GSPVEWVEEESYFFRLSAYGDRLLAHYEANPGfiLPAERRNEVASFVKSGLRDLSISRTtFDWGVP 218
Cdd:COG0143 161 LEPTELINPRsaisGAPPELREEEHYFFRLSKYQDRLLEWIEENPD--IQPEVRNEVLSWLKEGLQDLSISRD-FDWGIP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 219 VPNDPKHIMYVWVDALTNYLTAA-GYPDES--AERW-KYWPAD----IHMIGKDIVRFHAVYWPAFLMSADIELPKRVFA 290
Cdd:COG0143 238 VPGDPGKVFYVWFDALIGYISATkGYADDRglPEDFeKYWPAPdtelVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 291 HGFLFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFGSDGSYNHEAIVNRINADLANDLGNLAQRSLSMVAKN 370
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 371 CDGQVPAPGELTDEDNAILGAADALLDTSRAAMDDQAIHQMLNAVWQVVADANRYFAGQEPWALRKT-DPARMATVLYVT 449
Cdd:COG0143 398 FDGKVPEPGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDeDPERLATVLYTL 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839969221 450 IEVVRQVAILAQPVMPASSEKLLDLLGLHAEGRSFEQLGAygRLAAGTALPAPEGVFPRYVEKDEGA 516
Cdd:COG0143 478 LEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGW--PLPAGHKIGKPEPLFPRIEDEQIEA 542
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
6-508 |
0e+00 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 568.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 6 FYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWAT 85
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 86 LNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFDE-----------KETTLGED----GIRRE 150
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDryvegtcpkcgSEDARGDHcevcGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 151 PL----------GSPVEWVEEESYFFRLSAYGDRLLAHYEANPGFILPAERRNEVA-SFVKSGLRDLSISRTTFDWGVPV 219
Cdd:TIGR00398 161 PTelinprckicGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAqNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 220 PNDPKHIMYVWVDALTNYLTAAGYPDESAERW-KYWPAD-----IHMIGKDIVRFHAVYWPAFLMSADIELPKRVFAHGF 293
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISSLGILSGDTEDWkKWWNNDedaelIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 294 LFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFGSDGSYNHEAIVNRINADLANDLGNLAQRSLSMVAKNCDG 373
Cdd:TIGR00398 321 LTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKKYFNG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 374 QVPAPGELTDEDNAILGAADALLDTSRAAMDDQAIHQMLNAVWQVVADANRYFAGQEPWALRKTDPaRMATVLYVTIEVV 453
Cdd:TIGR00398 401 VLPSEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSP-RLKELLAVCSMLI 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1839969221 454 RQVAILAQPVMPASSEKLLDLLGLhaegrSFEQLGAYGRLaAGTALPAPEGVFPR 508
Cdd:TIGR00398 480 RVLSILLYPIMPKLSEKILKFLNF-----ELEWDFKLKLL-EGHKLNKAEPLFSK 528
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
5-339 |
1.04e-180 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 509.77 E-value: 1.04e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 5 TFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWA 84
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 85 TLNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFDekettlgedgirreplgspvEWVEEESY 164
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP--------------------EWREEEHY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 165 FFRLSAYGDRLLAHYEANPGFILPAERRNEVASFVKSGLRDLSISRTTFDWGVPVPNDPKHIMYVWVDALTNYLTAAGYP 244
Cdd:cd00814 141 FFRLSKFQDRLLEWLEKNPDFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPVPLDPGKVIYVWFDALIGYISATGYY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 245 DESAER----WKYWPADIHMIGKDIVRFHAVYWPAFLMSADIELPKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAKYGL 320
Cdd:cd00814 221 NEEWGNswwwKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGA 300
|
330
....*....|....*....
gi 1839969221 321 DAMRYYFLREVSFGSDGSY 339
Cdd:cd00814 301 DALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
6-363 |
4.42e-163 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 467.54 E-value: 4.42e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 6 FYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWAT 85
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 86 LNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFDEKETT--------LGEDGIRREPLGSPVE 157
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEgtcphcgsEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 158 ----------------WV-EEESYFFRLSAYGDRLLAHY-EANPGfiLPAERRNEVASFVKSGLRDLSISRtTFDWGVPV 219
Cdd:pfam09334 161 ptelinpkcvicgttpEVkETEHYFFDLSKFQDKLREWIeENNPE--WPENVKNMVLEWLKEGLKDRAISR-DLDWGIPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 220 PNDPKHIMYVWVDALTNYLTAAGYPDESAERWK-YWPAD-----IHMIGKDIVRFHAVYWPAFLMSADIELPKRVFAHGF 293
Cdd:pfam09334 238 PGAEGKVFYVWLDAPIGYISATKELSGNEEKWKeWWPNDpdtelVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGY 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 294 LFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFGSDGSYNHEAIVNRINADLANDLGNLAQRS 363
Cdd:pfam09334 318 LTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
5-508 |
1.49e-135 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 405.64 E-value: 1.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 5 TFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWA 84
Cdd:PLN02224 70 TFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 85 TLNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFDEKEttLGEDGIRrePLGS-PVEWVEEES 163
Cdd:PLN02224 150 DLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKE--LLENNCC--PVHQmPCVARKEDN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 164 YFFRLSAYGDRLLAHYEANPGFILPAERRNEVASFVKSGLRDLSISRTTFDWGVPVPNDPKHIMYVWVDALTNYLTAAGY 243
Cdd:PLN02224 226 YFFALSKYQKPLEDILAQNPRFVQPSYRLNEVQSWIKSGLRDFSISRALVDWGIPVPDDDKQTIYVWFDALLGYISALTE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 244 PD-----ESAERWKyWPADIHMIGKDIVRFHAVYWPAFLMSADIELPKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAKY 318
Cdd:PLN02224 306 DNkqqnlETAVSFG-WPASLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 319 GLDAMRYYFLREVSFGSDGSYNHEAIVNRINADLANDLGNLAQRSLSMVAKNCDGQVPAPGELTDEDNAILGAADALLDT 398
Cdd:PLN02224 385 GPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEK 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 399 SRAAMDDQAIHQMLNAVWQVVADANRYFAGQEPWALRK---TDPARMATVLYVTIEVVRQVAILAQPVMPASSEKLLDLL 475
Cdd:PLN02224 465 AQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKqggVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQL 544
|
490 500 510
....*....|....*....|....*....|....*..
gi 1839969221 476 GLHAEgrSFEQL----GAYGRLAAGTALPAPEGVFPR 508
Cdd:PLN02224 545 GYSED--QFNSItwsdTKWGGLKGGQVMEQASPVFAR 579
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
2-513 |
2.00e-108 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 337.51 E-value: 2.00e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 2 SRPTFyITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKD 81
Cdd:PRK00133 1 MRKIL-VTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 82 LWATLNISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSysgwysVRQeaFFDEKE---------------------- 139
Cdd:PRK00133 80 DFAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKT------IEQ--LYDPEKgmflpdrfvkgtcpkcgaedqy 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 140 --------TTLgedgirrEPL----------GSPVEWVEEESYFFRLSAYGDRLLaHYEANPGFiLPAERRNEVASFVKS 201
Cdd:PRK00133 152 gdncevcgATY-------SPTelinpksaisGATPVLKESEHFFFKLPRFEEFLK-EWITRSGE-LQPNVANKMKEWLEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 202 GLRDLSISRTTfDW-GVPVPNDPKHIMYVWVDALTNYL--TAAGYPDESAERWK-YWPAD-----IHMIGKDIVRFHAVY 272
Cdd:PRK00133 223 GLQDWDISRDA-PYfGFEIPGAPGKVFYVWLDAPIGYIssTKNLCDKRGGLDWDeYWKKDsdtelYHFIGKDIIYFHTLF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 273 WPAFLMSADIELPKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFG-SDGSYNHEAIVNRINAD 351
Cdd:PRK00133 302 WPAMLEGAGYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 352 LANDLGNLAQRSLSMVAKNCDGQVPApgelTDEDNAILGAADALLDTSRAAMDD----QAIHQMLNavwqvVAD-ANRYF 426
Cdd:PRK00133 382 LVGKVVNFASRTAGFINKRFDGKLPD----ALADPELLEEFEAAAEKIAEAYEArefrKALREIMA-----LADfANKYV 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 427 AGQEPWALRKTDPARMATVLYVTIEVVRQVAILAQPVMPASSEKLLDLLGLhaEGRSFEQLgayGRLAAGTALPAPEGVF 506
Cdd:PRK00133 453 DDNEPWKLAKQDGERLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNL--EELTWDDA---QQPLAGHPINKFKILF 527
|
....*..
gi 1839969221 507 PRyVEKD 513
Cdd:PRK00133 528 TR-IEDK 533
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
5-336 |
5.63e-86 |
|
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.
Pssm-ID: 185674 [Multi-domain] Cd Length: 312 Bit Score: 267.75 E-value: 5.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 5 TFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGI-------------APIEL 71
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 72 ATRNSQAFKDLWATLNISYD--DYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGwysvrqeaffdekettlgedgirr 149
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 150 eplgspvewVEEESYFFRLSAYGDRLLAHYEANPgfILPAERRNEVASFVKSGLrDLSISRTTFdWGVPVPNDpkhIMYV 229
Cdd:cd00668 137 ---------RITEQWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWLESLL-DWAISRQRY-WGTPLPED---VFDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 230 WVDALTNYLTAAGYPDESAERWKYWPADIHMIGKDIVRFHAVYWPAFLMSADIELP-KRVFAHGFLF-NRGEKMSKSVGN 307
Cdd:cd00668 201 WFDSGIGPLGSLGYPEEKEWFKDSYPADWHLIGKDILRGWANFWITMLVALFGEIPpKNLLVHGFVLdEGGQKMSKSKGN 280
|
330 340
....*....|....*....|....*....
gi 1839969221 308 VVDPFELVAKYGLDAMRYYFLREVSFGSD 336
Cdd:cd00668 281 VIDPSDVVEKYGADALRYYLTSLAPYGDD 309
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
348-475 |
5.03e-49 |
|
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.
Pssm-ID: 153411 [Multi-domain] Cd Length: 129 Bit Score: 164.97 E-value: 5.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 348 INADLANDLGNLAQRSLSMVAKNCDGQVPAPGELTDEDNAILGAADALLDTSRAAMDDQAIHQMLNAVWQVVADANRYFA 427
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1839969221 428 GQEPWALRKT-DPARMATVLYVTIEVVRQVAILAQPVMPASSEKLLDLL 475
Cdd:cd07957 81 ETAPWKLAKEeDPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
8-506 |
3.68e-45 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 169.58 E-value: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 8 ITTPIFYPNGVPHIGHAYTAIAS-DVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWATL 86
Cdd:PLN02610 21 ITSALPYVNNVPHLGNIIGCVLSaDVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 87 NISYDDYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQEAFFDEK--ETTLGEDGIRREP-----------LG 153
Cdd:PLN02610 101 DISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRlvEGTCPTEGCNYDSargdqcekcgkLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 154 SPVEWV--------------EEESYFFRLSAYGDRLLAHYEANPgfILPAERRNEVA---SFVKSGLRDLSISRTtFDWG 216
Cdd:PLN02610 181 NPTELIdpkckvckntprirDTDHLFLELPLLKDKLVEYINETS--VAGGWSQNAIQttnAWLRDGLKPRCITRD-LKWG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 217 VPVPND--PKHIMYVWVDALTNYLT-AAGYPDESAERWKYwPADIHM---IGKDIVRFHAVYWPAFLM--SADIELPKRV 288
Cdd:PLN02610 258 VPVPLEkyKDKVFYVWFDAPIGYVSiTACYTPEWEKWWKN-PENVELyqfMGKDNVPFHTVMFPSTLLgtGENWTMMKTI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 289 FAHGFLFNRGEKMSKSVGnvvdpfelVAKYGLDA---------MRYYFLREVSFGSDGSYNHEAIVNRINADLANDLGNL 359
Cdd:PLN02610 337 SVTEYLNYEGGKFSKSKG--------VGVFGNDAkdtnipvevWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 360 AQRSLSMVAKNC----DGQVP-APG-ELTDEDNAILGAADALLDTSRAAMDDQAIHQMLNAVWQVVADANRYFAGQEPWA 433
Cdd:PLN02610 409 INRVLSFIAKPPgagyGSVIPdAPGaESHPLTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 434 LRKTDPARMATVLYVTIEVVRQVAILAQPVMPASSEKLLDLLGLHAEGRSF-EQLGAYGR-------LAAGTALPAPEGV 505
Cdd:PLN02610 489 LYKEDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLsDEKGEVARakrpwelVPAGHKIGTPEPL 568
|
.
gi 1839969221 506 F 506
Cdd:PLN02610 569 F 569
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
6-328 |
1.02e-40 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 148.93 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 6 FYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWAT 85
Cdd:cd00812 2 FYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 86 LNISYD--DYIRTTEERHHKASQAIWNKMVEKGDIYLDsysgwysvrqeaffdekettlgedgirreplGSPVEW-VEEE 162
Cdd:cd00812 82 MGFSYDwrREFTTCDPEYYKFTQWLFLKLYEKGLAYKK-------------------------------EAPVNWcKLLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 163 SYFFRLS--AYGDRLLAHYEANPGFilPAErrnevasfVKSGLRD-LSISRTTFdWGVPVP-NDpkhIMYVWVDA----- 233
Cdd:cd00812 131 QWFLKYSetEWKEKLLKDLEKLDGW--PEE--------VRAMQENwIGCSRQRY-WGTPIPwTD---TMESLSDStwyya 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 234 --LTNYLTAAGYPDESA---ERWKYW-PADIHMIGKDIVRFH---AVYWPAFLMSADI---ELPKRVFAHGFLFNRGEKM 301
Cdd:cd00812 197 ryTDAHNLEQPYEGDLEfdrEEFEYWyPVDIYIGGKEHAPNHllySRFNHKALFDEGLvtdEPPKGLIVQGMVLLEGEKM 276
|
330 340
....*....|....*....|....*..
gi 1839969221 302 SKSVGNVVDPFELVAKYGLDAMRYYFL 328
Cdd:cd00812 277 SKSKGNVVTPDEAIKKYGADAARLYIL 303
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
4-336 |
2.66e-37 |
|
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 185677 [Multi-domain] Cd Length: 382 Bit Score: 141.23 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 4 PTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEK----EGIAP----------- 68
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEKklgiEGKTRhdlgreeflek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 69 -IELATRNSQAFKDLWATLNISYD--DYIRTTEERHHKASQAIWNKMVEKGDIYLDSY-SGWysvrqeaffDEK-ETTLG 143
Cdd:cd00817 81 cWEWKEESGGKIREQLKRLGASVDwsREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRlVNW---------CPKlRTAIS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 144 EDGIrREPLGSPVEWVEEESYFFRLSAYGDRLLAHYEANPGFILPAERRNEVASFVKSgLRDLSISRTTFdWGVPVP--- 220
Cdd:cd00817 152 DIEV-CSRSGDVIEPLLKPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLEN-IRDWCISRQLW-WGHRIPawy 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 221 -NDPKHimyvWVDALTNY------------------------------------LTAAGYPDESAERWKYWPADIHMIGK 263
Cdd:cd00817 229 cKDGGH----WVVAREEDeaidkaapeacvpcggeelkqdedvldtwfssslwpFSTLGWPEETKDLKKFYPTSLLVTGH 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1839969221 264 DIVRFHAVYWPAFLMSADIELP-KRVFAHGFLFN-RGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFGSD 336
Cdd:cd00817 305 DIIFFWVARMIMRGLKLTGKLPfKEVYLHGLVRDeDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQGRD 379
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
14-336 |
8.24e-31 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 122.34 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 14 YPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKE------------GIAPI-----ELATRNS 76
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKElgisgkkdiekmGIAEFnakcrEFALRYV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 77 QA-------------FKDLWATLNISYddyirttEErhhkasqAIWN---KMVEKGDIYLDSYsgwysvrqeaffdeket 140
Cdd:cd00818 91 DEqeeqfqrlgvwvdWENPYKTMDPEY-------ME-------SVWWvfkQLHEKGLLYRGYK----------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 141 tlgedgirrePLGSPVEWVEEESYFFRLSAYGDRLLahyEANPG--FIlPAERRNEVASFVKsGLRDLSISRTTFdWGVP 218
Cdd:cd00818 140 ----------VVPWPLIYRATPQWFIRVTKIKDRLL---EANDKvnWI-PEWVKNRFGNWLE-NRRDWCISRQRY-WGTP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 219 VP----NDPKHI--------MYVWVDALTNYLTAAGYPDESAERWKYWPADIHMIGKDIVR--FHAVywpafLMSADI-- 282
Cdd:cd00818 204 IPvwycEDCGEVlvrrvpdvLDVWFDSGSMPYAQLHYPFENEDFEELFPADFILEGSDQTRgwFYSL-----LLLSTAlf 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1839969221 283 -ELP-KRVFAHGF-LFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFGSD 336
Cdd:cd00818 279 gKAPyKNVIVHGFvLDEDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
4-471 |
6.47e-30 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 124.40 E-value: 6.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 4 PTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHG----QKMQQTAEKEGIAP----------- 68
Cdd:TIGR00422 33 PPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGiatqVKVEKKLGAEGKTKhdlgreefrek 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 69 -IELATRNSQAFKDLWATLNISYD---DYIrTTEERHHKASQAIWNKMVEKGDIYLDSY--------------------- 123
Cdd:TIGR00422 113 iWEWKEESGGTIKNQIKRLGASLDwsrERF-TMDEGLSKAVKEAFVRLYEKGLIYRGEYlvnwdpklntaisdieveyke 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 124 ---SGWYSVRQEAFFDEKE----TT------------------------------------------------------- 141
Cdd:TIGR00422 192 vkgKLYYIRYPLANGSKDYlvvaTTrpetmfgdtavavhpederykhligkkvilpltgrkipiiadeyvdmefgtgavk 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 142 -----------------------LGEDGIRREPLG------------SPVEWVEEESYFFRLS------AYGDR------ 174
Cdd:TIGR00422 272 vtpahdfndyewgkrhnlefiniLDEDGLLNENAGkyqgltrfearkKIVEDLKEEGLLVKIEphthnvGTCWRsgtvve 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 175 ------------------LLAHYEANPGFIlPAERRNEVASFVKSgLRDLSISRTTFdWGVPVP---------------- 220
Cdd:TIGR00422 352 pllskqwfvkvekladkaLEAAEEGEIKFV-PKRMEKRYLNWLRN-IKDWCISRQLI-WGHRIPvwyckecgevyvakee 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 221 ---NDPKHIMYV------------WVDALTNYLTAAGYPDESAERWKYWPADIHMIGKDIVRFHAVYWPAFLMSADIELP 285
Cdd:TIGR00422 429 plpDDKTNTGPSveleqdtdvldtWFSSSLWPFSTLGWPDETKDLKKFYPTDLLVTGYDIIFFWVARMIFRSLALTGQVP 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 286 -KRVFAHGFLFN-RGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFGSDGSYNHEAIVNriNADLANDLGNlAQRS 363
Cdd:TIGR00422 509 fKEVYIHGLVRDeQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVES--ARNFLNKLWN-ASRF 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 364 LSMVAKNCDGQVPAPGELTDEDNAILGAADALLDTSRAAMD----DQAIHQMLNAVWQVVADANRYFAGQEPWAlrkTDP 439
Cdd:TIGR00422 586 VLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDkyrfAEAAKALYEFIWNDFCDWYIELVKYRLYN---GNE 662
|
650 660 670
....*....|....*....|....*....|..
gi 1839969221 440 ARMATVLYVTIEVVRQVAILAQPVMPASSEKL 471
Cdd:TIGR00422 663 AEKKAARDTLYYVLDKALRLLHPFMPFITEEI 694
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
3-421 |
6.07e-21 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 96.80 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 3 RPTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHG----QKMQqtaEKEGIAP---------- 68
Cdd:PRK13208 37 KPVYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGlpteRKVE---KYYGIRKddisreefie 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 69 --IELATRNSQAFKDLWATLNISYD--DYIRTTEERHHKASQAIWNKMVEKGDIYLDSYSGWYSVRQE---AF----FDE 137
Cdd:PRK13208 114 lcRELTDEDEKKFRELWRRLGLSVDwsLEYQTISPEYRRISQKSFLDLYKKGLIYRAEAPVLWCPRCEtaiAQaeveYRE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 138 KETTL--------GEDGI-----RREPLGSPVEWV---EEESY------FFRLSAYGDR--LLAHYEANP---------- 183
Cdd:PRK13208 194 REGKLnyikfpveDGEEIeiattRPELLPACVAVVvhpDDERYkhlvgkTAIVPLFGVEvpILADPLVDPdfgtgavmic 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 184 -------------------------GFILPA----------ERRNEVASFVKSG-------------------------- 202
Cdd:PRK13208 274 tfgdktdvtwwrelnlptriiidedGRMTEAagklagltieEARKKIVEDLKSGgllgkqepikhnvkfcercdtpleil 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 203 ------LRDLS-----------------------------------ISRTTFdWGVPVP-------------------ND 222
Cdd:PRK13208 354 vtrqwfIKVLDlkeellergkeinwypehmrvrlenwieglnwdwcISRQRY-FGTPIPvwyckdcghpilpdeedlpVD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 223 P---------------------KHIMYVWVD-ALTnYLTAAGYPDESAERWKYWPADIHMIGKDIVRFHAVYwpAFLMSA 280
Cdd:PRK13208 433 PtkdeppgykcpqcgspgfegeTDVMDTWATsSIT-PLIVTGWERDEDLFEKVFPMDLRPQGHDIIRTWLFY--TILRAY 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 281 DI--ELP-KRVFAHGFLFN-RGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLrEVSFGSDGSYNhEAIVnRINADLANDL 356
Cdd:PRK13208 510 LLtgKLPwKNIMISGMVLDpDGKKMSKSKGNVVTPEELLEKYGADAVRYWAA-SARLGSDTPFD-EKQV-KIGRRLLTKL 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1839969221 357 GNLAQRSLSMVAKNCDgqvPAPGELTDEDNAILGAADALLDTSRAAMD----DQAIHQMLNAVWQVVAD 421
Cdd:PRK13208 587 WNASRFVLHFSADPEP---DKAEVLEPLDRWILAKLAKVVEKATEALEnydfAKALEEIESFFWHVFCD 652
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
242-483 |
1.42e-15 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 79.71 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 242 GYPDESAERWKYWPADIHMIGKDIVRFhavyWPA-------FLMSadiELP-KRVFAHGFLfnR---GEKMSKSVGNVVD 310
Cdd:COG0525 462 GWPEKTEDLKYFYPTSVLVTGFDIIFF----WVArmimmglHFTG---EVPfKDVYIHGLV--RdeqGRKMSKSKGNVID 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 311 PFELVAKYGLDAMRYYFLREVSFGSDgsynheaivnrINADL---------ANDLGNlAQRSLSMvakNCDGQV----PA 377
Cdd:COG0525 533 PLDLIDKYGADALRFTLAALASPGRD-----------IKFDEervegyrnfANKLWN-ASRFVLM---NLEGFDpgldPD 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 378 PGELTDEDNAILGAADALLDTSRAAMDDQAIHQMLNA----VWQVVADanryfagqepW-------ALRKTDPARMATVL 446
Cdd:COG0525 598 PEELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQAlydfVWNEFCD----------WylelakpRLYGGDEAAKRETR 667
|
250 260 270
....*....|....*....|....*....|....*..
gi 1839969221 447 YVTIEVVRQVAILAQPVMPASSEKLLDLLGLHAEGRS 483
Cdd:COG0525 668 ATLVYVLEQILRLLHPFMPFITEEIWQKLPPRKEGES 704
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
242-475 |
5.42e-15 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 78.11 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 242 GYPDESAERWKYWPADIHMIGKDIVRFhavyWPAFLMSADI----ELPKR-VFAHGFLFN-RGEKMSKSVGNVVDPFELV 315
Cdd:PRK14900 478 GWPEQTDTLRTFYPTSVMETGHDIIFF----WVARMMMMGLhfmgEVPFRtVYLHPMVRDeKGQKMSKTKGNVIDPLVIT 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 316 AKYGLDAMRYYFLREVSFGSDGSYNHEAIVNRinADLANDLGNLAQRSL-SMVAKNCDGQVPAPGELTDEDNAILGAADA 394
Cdd:PRK14900 554 EQYGADALRFTLAALTAQGRDIKLAKERIEGY--RAFANKLWNASRFALmNLSGYQERGEDPARLARTPADRWILARLQR 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 395 LLDTSRAAMDDQAIHQMLNAVWQVV-ADANRYFAGQEPWALRKTDPARMATVLYVTIEVVRQVAILAQPVMPASSEKLLD 473
Cdd:PRK14900 632 AVNETVEALEAFRFNDAANAVYAFVwHELCDWYIELAKEALASEDPEARRSVQAVLVHCLQTSYRLLHPFMPFITEELWH 711
|
..
gi 1839969221 474 LL 475
Cdd:PRK14900 712 VL 713
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
242-471 |
1.05e-13 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 73.99 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 242 GYPDESAERWKYWPADIHMIGKDIVRFhavyWPA-------FLMSadiELP-KRVFAHGFLfnR---GEKMSKSVGNVVD 310
Cdd:PRK05729 460 GWPEKTEDLKRFYPTSVLVTGFDIIFF----WVArmimmglHFTG---QVPfKDVYIHGLV--RdeqGRKMSKSKGNVID 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 311 PFELVAKYGLDAMRYYFLREVSFGSDGSYNHEaivnRINA--DLANDLGNlAQRSLSM-VAKNCDGQVPAPGELTDEDNA 387
Cdd:PRK05729 531 PLDLIDKYGADALRFTLAALASPGRDIRFDEE----RVEGyrNFANKLWN-ASRFVLMnLEGADVGELPDPEELSLADRW 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 388 ILGAADALLDTSRAAMDDQAIHQMLNA----VWQVVADanryfagqepWALRKTDP----ARMATVLYVTIEVVRQVAIL 459
Cdd:PRK05729 606 ILSRLNRTVAEVTEALDKYRFDEAARAlyefIWNEFCD----------WYLELAKPvlqeAAKRATRATLAYVLEQILRL 675
|
250
....*....|..
gi 1839969221 460 AQPVMPASSEKL 471
Cdd:PRK05729 676 LHPFMPFITEEL 687
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
2-177 |
3.09e-13 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 72.55 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 2 SRPTFYITTPIFYPNGVP-HIGH--AYTAiaSDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQA 78
Cdd:PLN02563 108 SKPKFYVLDMFPYPSGAGlHVGHpeGYTA--TDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIAR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 79 FKDLWATLNISYD--DYIRTTEERHHKASQAIWNKMVEKGDIYLDSYS-GWYSVRQEAFFDEKETtlgeDGIrREPLGSP 155
Cdd:PLN02563 186 FRSQLKSLGFSYDwdREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPvNWCPALGTVLANEEVV----DGL-SERGGHP 260
|
170 180
....*....|....*....|..
gi 1839969221 156 VEWVEEESYFFRLSAYGDRLLA 177
Cdd:PLN02563 261 VIRKPMRQWMLKITAYADRLLE 282
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
8-84 |
4.03e-13 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 66.73 E-value: 4.03e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839969221 8 ITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWA 84
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVE 77
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
286-465 |
2.39e-12 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 69.72 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 286 KRVFAHGF-LFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLReVSFGSDGSYNHEaIVNRInADLANDLGNLAqRSL 364
Cdd:COG0060 588 KNVLTHGFvLDEDGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS-SDYWGDLRFSDE-ILKEV-RDVYRRLRNTY-RFL 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 365 SMvakNCDG-----QVPAPGELTDEDNAILGAADALLDTSRAAMDDQAIHQMLNAVWQVVADA--NRY-------Fagqe 430
Cdd:COG0060 664 LA---NLDDfdpaeDAVPYEDLPELDRWILSRLNELIKEVTEAYDNYDFHRAYRALHNFCVEDlsNWYldiskdrL---- 736
|
170 180 190
....*....|....*....|....*....|....*..
gi 1839969221 431 pWALRKTDPARMA--TVLYvtiEVVRQVAILAQPVMP 465
Cdd:COG0060 737 -YTEAADSLDRRAaqTTLY---EVLETLVRLLAPILP 769
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
226-328 |
5.82e-12 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 68.21 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 226 IMYVWVD-ALTNYLTAaGYPDESAERWK-YWPADIHMIGKDIVRFhavyWPAFLMSADIEL----P-KRVFAHGFLFN-R 297
Cdd:pfam00133 486 VLDTWFSsGSWPFSTL-GWPFVNTEEFKkFFPADMLLEGSDQTRG----WFYRMIMLSTALtgsvPfKNVLVHGLVRDeQ 560
|
90 100 110
....*....|....*....|....*....|.
gi 1839969221 298 GEKMSKSVGNVVDPFELVAKYGLDAMRYYFL 328
Cdd:pfam00133 561 GRKMSKSLGNVIDPLDVIDKYGADALRLWLA 591
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
126-325 |
1.95e-11 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 66.89 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 126 WYSVRQEAFFDEKETTLGedgIRREPL----------GSPVEWVEEESYFFRLSAYGDRLLAHYEANPGFILPaERRNEV 195
Cdd:PLN02943 365 WFEAREKLWSDLEETGLA---VKKEPHtlrvprsqrgGEVIEPLVSKQWFVTMEPLAEKALKAVENGELTIIP-ERFEKI 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 196 ASFVKSGLRDLSISRTTFdWGVPVP--------NDPKHI---------------------MYVWVDALTNYLTAA----- 241
Cdd:PLN02943 441 YNHWLSNIKDWCISRQLW-WGHRIPvwyivgkdCEEDYIvarsaeealekarekygkdveIYQDPDVLDTWFSSAlwpfs 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 242 --GYPDESAERWK-YWPADIHMIGKDIVRFhavyWPAFLMSADIE----LP-KRVFAHGFLFN-RGEKMSKSVGNVVDPF 312
Cdd:PLN02943 520 tlGWPDVSAEDFKkFYPTTVLETGHDILFF----WVARMVMMGIEftgtVPfSYVYLHGLIRDsQGRKMSKTLGNVIDPL 595
|
250
....*....|...
gi 1839969221 313 ELVAKYGLDAMRY 325
Cdd:PLN02943 596 DTIKEFGTDALRF 608
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
4-119 |
1.89e-10 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 63.20 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 4 PTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKE------------GIAPI-- 69
Cdd:pfam00133 23 PSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEKKlgikekktrhkyGREEFre 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1839969221 70 ---ELATRNSQAFKDLWATLNISYD---DYIrTTEERHHKASQAIWNKMVEKGDIY 119
Cdd:pfam00133 103 kcrEWKMEYADEIRKQFRRLGRSIDwdrEYF-TMDPELEAAVWEVFVRLHDKGLIY 157
|
|
| Anticodon_3 |
pfam19303 |
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ... |
375-506 |
5.35e-10 |
|
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ligase. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 437135 [Multi-domain] Cd Length: 152 Bit Score: 57.90 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 375 VPAPGELTDEDNAILGAADALLDTSRAAMDdqAIH-----QMLNAVWqvVAdANRYFAGQEPWALRKTDPARMATVLYVT 449
Cdd:pfam19303 1 VPEGGAYGEAEAALIADLTTRLAAYEGHME--AMEvrkaaAELRAIW--VA-GNEYLQEAAPWTTFKTDPEAAAAQVRLA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1839969221 450 IEVVRQVAILAQPVMPASSEKLLDllGLHAEGRSF--EQLGAYGRLAAGTALPAPEGVF 506
Cdd:pfam19303 76 LNLIRLYAVLSAPFIPDAAAAMLA--AMGTDDAAWpdDVAAALTALPAGHAFTVPEVLF 132
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
2-177 |
1.34e-08 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 57.75 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 2 SRPTFYITT--PifYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAF 79
Cdd:COG0495 31 SKPKYYVLDmfP--YPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLHPMGWDAFGLPAENAAIKNGVHPAEWTYENIANM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 80 KDLWATLNISYD-DY-IRTTEERHHKASQAIWNKMVEKGDIYldsysgwysvRQEAF--FDEK-ETTLG----EDGiRRE 150
Cdd:COG0495 109 RRQLKRLGLSYDwSReIATCDPEYYKWTQWIFLQLYEKGLAY----------RKEAPvnWCPVdQTVLAneqvIDG-RCW 177
|
170 180
....*....|....*....|....*..
gi 1839969221 151 PLGSPVEWVEEESYFFRLSAYGDRLLA 177
Cdd:COG0495 178 RCGAPVEKKELPQWFLKITDYADELLD 204
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
19-93 |
6.05e-08 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 53.35 E-value: 6.05e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839969221 19 PHIGHAYTAIASDVIARFHRLDGKDVFF---LTGTDEhgqKMQQTAEKEGIAPIELATRNSQAFKDLWATLNISYDDY 93
Cdd:cd00672 34 AHIGHARTYVVFDVLRRYLEDLGYKVRYvqnITDIDD---KIIKRAREEGLSWKEVADYYTKEFFEDMKALNVLPPDV 108
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
288-326 |
7.18e-08 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 55.06 E-value: 7.18e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1839969221 288 VFAHGFLFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYY 326
Cdd:COG0495 577 VGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLF 615
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
242-315 |
4.35e-07 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 52.70 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 242 GYPDESAERWKYWPADIHMIGKDIVRFhavyWPA--FLMSADI--ELP-KRVFAHGFLFN-RGEKMSKSVGNVVDPFELV 315
Cdd:PTZ00419 525 GWPDQTDDLQRFFPTSLLETGSDILFF----WVArmVMMSLHLtdKLPfKTVFLHAMVRDsQGEKMSKSKGNVIDPLEVI 600
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
238-323 |
1.21e-06 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 51.44 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 238 LTAAGYPDESAERWKYWPADIHMIGKDIVRFhavyWPAFLMSADIELP-----KRVFAHGFLFN-RGEKMSKSVGNVVDP 311
Cdd:PLN02381 591 LSVLGWPDDTDDLKAFYPTSVLETGHDILFF----WVARMVMMGMQLGgdvpfRKVYLHPMIRDaHGRKMSKSLGNVIDP 666
|
90
....*....|..
gi 1839969221 312 FELVAKYGLDAM 323
Cdd:PLN02381 667 LEVINGISLEGL 678
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
187-324 |
1.54e-06 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 50.93 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 187 LPAERRNEVASFVkSGLRDLSISRTTfDWGVPVP-------NDP-------KHI-------------------------- 226
Cdd:PLN02843 451 IPAQGENRIRAMV-SGRSDWCISRQR-TWGVPIPvfyhvetKEPlmneetiAHVksivaqkgsdawwymdvedllpekyr 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 227 ------------MYVWVDALTNYLTAAGYPDESAerwkyWPADIHMIGKDIVR--FHAvywpAFLMS--ADIELP-KRVF 289
Cdd:PLN02843 529 dkasdyekgtdtMDVWFDSGSSWAGVLGSREGLS-----YPADLYLEGSDQHRgwFQS----SLLTSvaTKGKAPyKSVL 599
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1839969221 290 AHGFLFN-RGEKMSKSVGNVVDPFELV-----AK----YGLDAMR 324
Cdd:PLN02843 600 THGFVLDeKGFKMSKSLGNVVDPRLVIeggknQKqepaYGADVLR 644
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
19-88 |
2.47e-06 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 50.10 E-value: 2.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1839969221 19 PHIGHAYTAIASDVIARFHRLDGKDVFF---LTGTDEhgqKMQQTAEKEGIAPIELATRNSQAFKDLWATLNI 88
Cdd:COG0215 36 AHIGHARTFVVFDVLRRYLRYLGYKVTYvrnITDVDD---KIIKRAAEEGESIWELAERYIAAFHEDMDALGV 105
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
15-51 |
5.61e-06 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 49.33 E-value: 5.61e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1839969221 15 PN--GVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTD 51
Cdd:PRK05729 45 PNvtGSLHMGHALNNTLQDILIRYKRMQGYNTLWLPGTD 83
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
5-328 |
6.78e-06 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 48.13 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 5 TFYITTPIFYpnGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKEGIAPIELATRNSQAFKDLWA 84
Cdd:pfam01406 11 TMYVCGPTVY--DYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 85 TLNISYDD-YIRTTEerHHKASQAIWNKMVEKGDIYL----DSYsgwYSVRQEAFFdekettlgedgirreplGSPVEWV 159
Cdd:pfam01406 89 ALNVLPPDlEPRVTE--HIDEIIEFIERLIKKGYAYVsdngDVY---FDVSSFPDY-----------------GKLSGQN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 160 EEEsyffrlsaygdrllahyeanpgfiLPAERRNEVaSFVKSGLRDLSIsrttfdWGVPVPNDPKhimyvWVDALtnylt 239
Cdd:pfam01406 147 LEQ------------------------LEAGARGEV-SEGKRDPLDFAL------WKASKEGEPS-----WDSPW----- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 240 AAGYP----DESAERWKYW--PADIHMIGKDIVRFHAVYWPAFLMSA-DIELPKRVFAHGFLFNRGEKMSKSVGNVVDPF 312
Cdd:pfam01406 186 GKGRPgwhiECSAMARKYLgdQIDIHGGGIDLAFPHHENEIAQSEAAfDKQLANYWLHNGHVMIDGEKMSKSLGNFFTIR 265
|
330
....*....|....*.
gi 1839969221 313 ELVAKYGLDAMRYYFL 328
Cdd:pfam01406 266 DVLKRYDPEILRYFLL 281
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
15-64 |
7.69e-06 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 48.85 E-value: 7.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1839969221 15 PN--GVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKE 64
Cdd:PTZ00419 69 PNvtGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGIATQVVVEKK 120
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
3-72 |
1.04e-05 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 48.15 E-value: 1.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1839969221 3 RPTFyittpIF-----YPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQkmqqtaekegiaPIELA 72
Cdd:COG0060 45 RPKF-----VLhdgppYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGL------------PIELK 102
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
293-326 |
1.28e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 47.90 E-value: 1.28e-05
10 20 30
....*....|....*....|....*....|....
gi 1839969221 293 FLFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYY 326
Cdd:PLN02563 716 RLIARAHKMSKSRGNVVNPDDVVSEYGADSLRLY 749
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
253-325 |
2.47e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 46.99 E-value: 2.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839969221 253 YW-PADIHMIGKDIVRFH---AVYWPAFLMsADIELPKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAKYGLDAMRY 325
Cdd:PLN02959 668 YWyPFDLRVSGKDLIQNHltfAIYNHTAIW-AEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRF 743
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
291-329 |
2.74e-05 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 46.63 E-value: 2.74e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1839969221 291 HGFLFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLR 329
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLS 294
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
287-328 |
3.80e-05 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 44.88 E-value: 3.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1839969221 287 RVFAH-GFLFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFL 328
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALL 202
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
2-64 |
6.93e-05 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 45.66 E-value: 6.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1839969221 2 SRPTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTDEHGQKMQQTAEKE 64
Cdd:PLN02381 126 SKPPFVIVLPPPNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKK 188
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
19-50 |
7.32e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 45.63 E-value: 7.32e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1839969221 19 PHIGHAYTAIASDVIARFHRLDGKDVFF-----LTGT 50
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFpmafhVTGT 37
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
253-326 |
1.21e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 44.86 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 253 YW-PADIHMIGKDIVR-------FHAV------YWPaflmsadielpKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAKY 318
Cdd:PRK12300 527 YWyPVDWRHSGKDLIPnhltffiFNHVaifpeeKWP-----------RGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEY 595
|
....*...
gi 1839969221 319 GLDAMRYY 326
Cdd:PRK12300 596 GADVVRLY 603
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
243-326 |
2.70e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 43.95 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 243 YPDESAERW-KYWPADIHMIGKDIVRfhavYWPAFLM---SADIELP--KRVFAHGF-LFNRGEKMSKSVGNVVDPFELV 315
Cdd:PLN02882 554 YPFENKELFeKNFPADFVAEGLDQTR----GWFYTLMvlsTALFDKPafKNLICNGLvLAEDGKKMSKSLKNYPDPNEVI 629
|
90
....*....|.
gi 1839969221 316 AKYGLDAMRYY 326
Cdd:PLN02882 630 DKYGADALRLY 640
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
15-51 |
2.94e-04 |
|
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440291 [Multi-domain] Cd Length: 877 Bit Score: 43.50 E-value: 2.94e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1839969221 15 PN--GVPHIGHAYTAIASDVIARFHRLDGKDVFFLTGTD 51
Cdd:COG0525 44 PNvtGSLHMGHALNNTLQDILIRYKRMQGYNTLWQPGTD 82
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
4-46 |
4.48e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 43.13 E-value: 4.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1839969221 4 PTFYITTPIFYPNGVPHIGHAYTAIASDVIARFHRLDGKDVFF 46
Cdd:PLN02959 45 EKFFGNFPYPYMNGLLHLGHAFSLSKLEFAAAYHRLRGANVLL 87
|
|
| MaoC_C |
cd03452 |
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ... |
264-334 |
4.64e-04 |
|
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.
Pssm-ID: 239536 [Multi-domain] Cd Length: 142 Bit Score: 40.46 E-value: 4.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1839969221 264 DIVRFHAVYWPAFLMSADIE------LPKRVfAHGFLFnrgekMSKSVGNVVDPFE--LVAKYGLDAMRyyFLREVSFG 334
Cdd:cd03452 22 DIVNFACLTGDHFYAHMDEIaakasfFGKRV-AHGYFV-----LSAAAGLFVDPAPgpVLANYGLENLR--FLEPVYPG 92
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
250-329 |
2.46e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 40.00 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839969221 250 RWKYWPADIHMIGKDivrfHAVYWPAFLMSADI-------ELPKRVFAHGFLFNRGEKMSKSVGNVVDPFELVAKYGLDA 322
Cdd:cd00674 222 RWAILGVDFEPFGKD----HASAGGSYDTGKEIareifggEPPVPVMYEFIGLKGGGKMSSSKGNVITPSDWLEVAPPEV 297
|
....*..
gi 1839969221 323 MRYYFLR 329
Cdd:cd00674 298 LRYLYAR 304
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
294-348 |
2.80e-03 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 40.72 E-value: 2.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1839969221 294 LFNRGEKMSKSVGNVVDPFELVAKYGLDAMRYYFLREVSFGSDGSYNHEAIVNRI 348
Cdd:PTZ00427 714 LASDGKKMSKRLKNYPDPLYILDKYGADSLRLYLINSVAVRAENLKFQEKGVNEV 768
|
|
| |
